ArticleProteomics2006
A global proteomics approach identifies novel phosphorylated signaling proteins in GPVI-activated platelets: involvement of G6f, a novel platelet Grb2-binding membrane adapter.
Article in Proteomics, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
24 citing papers in PubMed, 92 citations in OpenAlex.
- Trial
- Advances and Trends in Omics Technology Development.Frontiers in medicine · 2022Review
- Proteomics: A Tool to Study Platelet Function.International journal of molecular sciences · 2021Review
- Platelets in Healthy and Disease States: From Biomarkers Discovery to Drug Targets Identification by Proteomics.International journal of molecular sciences · 2020Review
- Comparative proteomics reveals unexpected quantitative phosphorylation differences linked to platelet activation state.Scientific reports · 2019Article
- Article
- Alteration of platelet GPVI signaling in ST-elevation myocardial infarction patients demonstrated by a combination of proteomic, biochemical, and functional approaches.Scientific reports · 2016Article
- HBV maintains electrostatic homeostasis by modulating negative charges from phosphoserine and encapsidated nucleic acids.Scientific reports · 2016Article
- Breaking the mold: transcription factors in the anucleate platelet and platelet-derived microparticles.Frontiers in immunology · 2015Review
- Global proteome analysis identifies active immunoproteasome subunits in human platelets.Molecular & cellular proteomics : MCP · 2014Article
- Growth factor receptor-bound protein 2 contributes to (hem)immunoreceptor tyrosine-based activation motif-mediated signaling in platelets.Circulation research · 2014Article
- Phosphoproteomic analysis of platelets activated by pro-thrombotic oxidized phospholipids and thrombin.PloS one · 2014Article
- Response to "Platelets proteomics in transfusion medicine: a reality with challenging but promising future".Blood transfusion = Trasfusione del sangue · 2013Article
- Article
- Proteome changes in platelets activated by arachidonic acid, collagen, and thrombin.Proteome science · 2010Article
- Proteins involved in platelet signaling are differentially regulated in acute coronary syndrome: a proteomic study.PloS one · 2010Article
- A molecule in teleost fish, related with human MHC-encoded G6F, has a cytoplasmic tail with ITAM and marks the surface of thrombocytes and in some fishes also of erythrocytes.Immunogenetics · 2010Article
- Article
- Proteomic and metabolomic profiles in atherothrombotic vascular disease.Current atherosclerosis reports · 2010Review
- Proteomic and phospho-proteomic profile of human platelets in basal, resting state: insights into integrin signaling.PloS one · 2009Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
Collagen-related peptide (CRP) stimulates powerful activation of platelets through the glycoprotein VI (GPVI)-FcR gamma-chain complex. We have combined proteomics and traditional biochemistry approaches to study the proteome of CRP-activated platelets, focusing in detail on tyrosine phosphorylation. In two separate approaches, phosphotyrosine immunoprecipitations followed by 1-D-PAGE, and 2-DE, were used for protein separation. Proteins were identified by MS. By following these approaches, 96 proteins were found to undergo PTM in response to CRP in human platelets, including 11 novel platelet proteins such as Dok-1, SPIN90, osteoclast stimulating factor 1, and beta-Pix. Interestingly, the type I transmembrane protein G6f was found to be specifically phosphorylated on Tyr-281 in response to platelet activation by CRP, providing a docking site for the adapter Grb2. G6f tyrosine phoshporylation was also found to take place in response to collagen, although not in response to the G protein-coupled receptor agonists, thrombin and ADP. Further, we also demonstrate for the first time that Grb2 and its homolog Gads are tyrosine-phosphorylated in CRP-stimulated platelets. This study provides new insights into the mechanism of platelet activation through the GPVI collagen receptor, helping to build the basis for the development of new drug targets for thrombotic disease.
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.